Recombinant Human Antithrombin-III (SERPINC1)

Code CSB-MP021079HU(M4)
Size $660
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Greater than 85% as determined by SDS-PAGE.
Target Names
Uniprot No.
Research Area
Alternative Names
Serpin C1
Homo sapiens (Human)
Mammalian cell
Expression Region
Target Protein Sequence
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
54.8 kDa
Protein Length
Full Length
Tag Info
N-terminal 6xHis-tagged
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
18-28 business days
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

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Target Background

Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin.
Gene References into Functions
  1. Molecular analysis may be the best method to identify antithrombin deficiency. Up to 80% of patients with antithrombin deficiency have SERPINC1 gene defects, mostly (90% of the 315 gene defects described so far) point mutations or small deletions or insertions affecting the 7 exons or flanking regions. [review] PMID: 30005274
  2. Laboratory tests and direct sequencing of PROC and SERPINC1 were conducted for the patient and his family members. Coagulation tests revealed that the patient presented type I antithrombin deficiency combined with decreased protein C activity resulting from a small insertion mutation c.848_849insGATGT in SERPINC1 and a short deletion variant c.572_574delAGA in PROC. PMID: 28861852
  3. Thirty-one members of a single family were included. Clinical data was collected regarding thrombotic history. The mutation was identified by direct sequencing of the SERPINC1 gene. HEK293 cells were transfected with wild type and mutant SERPINC1 plasmids. PMID: 28783511
  4. the first report of regulatory region polymorphisms in SERPINC1 gene in Indian population PMID: 27279637
  5. this study shows that risk for thrombosis is associated with the different SERPINC1 genotypes PMID: 28300866
  6. Report high levels of latent antithrombin in plasma from patients with antithrombin deficiency caused by mutations affecting the stability of the native conformation. PMID: 28229161
  7. Study identified one new small deletion within AT, which results in the loss of four amino acids (INEL) and is located at strand 3 of beta-sheet A, a region highly conserved in SERPINC1. This mutation leads to type I AT deficiency by promoting the intracellular retention of AT, which induces ER stress. PMID: 27708219
  8. It was our aim to identify mutations in SERPINC1 causing transient antithrombin deficiency. SERPINC1 was sequenced in 214 cases with a positive test for antithrombin deficiency, including 67 with no deficiency in the sample delivered to our laboratory. The p.Val30Glu mutation (Antithrombin Dublin) was identified in five out of these 67 cases, as well as in three out of 127 cases with other SERPINC1 mutations. PMID: 27098529
  9. different types of SERPINC1 mutations may play different roles in the development of VTE PMID: 27863268
  10. aberrant N-glycosylation causing a recessive or transient antithrombin deficiency is a new form of thrombophilia that does not have a SERPINC1 gene defect PMID: 27214821
  11. The results this study reveal several novel mutations to the already growing list of SERPINC1 mutations, thereby adding to our knowledge of the molecular background of antithrombin deficiency. PMID: 28317092
  12. Data indicate that all patients suffered from homozygous antithrombin (AT) deficiency caused by the mutation p.Leu131Phe in the AT gene (SERPINC1). PMID: 28361296
  13. Studies indicate that antithrombin III (ATIII) and its gene SerpinC1 may be related to many diseases, including hypertension and kidney diseases. PMID: 28424376
  14. The odds ratio of developing idiopathic fatal pulmonary embolism as a variant carrier for SERPINC1 is 144.2 (95% CI, 26.3-779.4; P = 1.7 x 10- 7). PMID: 28174134
  15. Nine patients (1.8%), [5% in arterial thrombosis and 0.8% in venous thrombosis] showed a missense variant in exon 5 i.e. p.Pro305His (c.1033 C > A); none of these patients showed the presence of any other variations in the gene. PMID: 27161325
  16. In Hungary, the founder mutation, ATBp3, is the most common Antithrombin deficiency PMID: 26748602
  17. Our studies of ATIII in-cell folding reveal a surprising, biased order of disulfide bond formation, with early formation of the C-terminal disulfide, before formation of the N-terminal disulfides, critical for folding to the active, metastable state PMID: 27222580
  18. Describe antibody specifically targeting a unique conformational epitope on antithrombin III beta conformation that blocks anticoagulation. PMID: 26581031
  19. This is the first case of pregnancy related stroke, associated with type-II heparin binding site antithrombin deficiency (c. 391C > T, p.Leu131Phe), that has been reported so far. A genetic analysis of the AT gene (SERPINC1) was performed. PMID: 26916305
  20. The present study highlights that AT physiological activities are strictly controlled not only by a core fucose at the reducing end but also by the high-mannose-type structures at the nonreducing end. The beta-form with the immature high-mannose type appears to function as a more potent anticoagulant than the AT typically found in human plasma, once it emerges in the blood. PMID: 26747427
  21. Elevated levels of circulating microparticles can play a role in carriers of mild and severe inherited thrombophilia resulting from antithrombin deficiency. PMID: 26354831
  22. The relevance of the vitamin D pathway on the regulation of SERPINC1 was confirmed in a cell model. PMID: 27003919
  23. The increased SERPINC1 SNP frequency among Han patients receiving heart surgery might contribute to the differences in their perioperative sensitivity to heparin PMID: 25361738
  24. Patients with low antithrombin III activities presented a higher risk of developing acute kidney injury after cardiac surgery. PMID: 26108065
  25. Letter/Case Report: novel antithrombin mutation resulting in antithrombin deficiency and arterial/venous thrombosis. PMID: 26177694
  26. Report antirhtombin III levels were negatively correlated with gestational age during third trimester of pregnancy, and fall further immediately after childbirth. PMID: 25087890
  27. This suggests that allosteric information propagation pathways are present even in the non-activated native form of antithrombin. PMID: 25483839
  28. analysis of mutations in SERPINC1 with a role in Hereditary antithrombin (AT) deficiency PMID: 25837307
  29. Polymorphisms in factor V and antithrombin III gene in recurrent pregnancy loss PMID: 25771983
  30. this is the first report of AT mutations in SERPINC1 gene in Indo-Aryan population where a novel point mutation p.T280A and a novel single nucleotide insertion g.13362_13363insA are reported. PMID: 25811371
  31. Selective disruption of exosite-mediated regulation of factor IX by heparin and antithrombin can be achieved with preserved or enhanced thrombin generation capacity. PMID: 25851619
  32. report of a large in-frame deletion causing antithrombin deficiency PMID: 25298121
  33. c.1058C>T variant in the SERPINC1 gene is pathogenic for antithrombin deficiency. PMID: 25522812
  34. We identified a novel hereditary mutation, g.1267G>A (p.A391T), in the AT gene, which reduces its heparin binding capacity and might be associated with resistance to heparin PMID: 25312341
  35. We posit that active site adduction is the mechanism of MGO-mediated inhibition of ATIII, and thus contributes to the underlying pathophysiology of the diabetic hypercoagulable state and complications thereof. PMID: 25307422
  36. prevalence of mutations in a cohort of pediatric patients with venous thromboembolism is reported PMID: 24966143
  37. AT-p.Ala416Pro mutation was responsible for type IIa AT deficiency in the family. PMID: 24583439
  38. genetic polymorphism affects endogenous thrombin potential among FV Leiden carriers PMID: 24226152
  39. The type of inherited AT defect modulates not only the risk of thromboembolism but also the localisation. PMID: 24196373
  40. data showed heterozygous mutations of c.2534C>T (R56C), c.13398C>A (A459D) and c.2703C>G (P112R) in the AT gene caused antithrombin (AT) deficiency in 3 unrelated Japanese pedigrees; findings suggest the A459D and P112R mutants are responsible for type I AT deficiency PMID: 23809926
  41. Mutation in SERPINC1 is associated with inherited homozygous antithrombin deficiency PMID: 24072242
  42. Rare double heterozygous mutations in antithrombin underlie hereditary thrombophilia in a Chinese family PMID: 23117546
  43. Data indicate that in patients on haemodialysis, thrombin-antithrombin (TAT) levels were increased and inversely correlated with primary assisted patency and secondary patency. PMID: 23844096
  44. The allosteric mechanism of activation of antithrombin as an inhibitor of factor IXa and factor Xa: heparin-independent full activation through mutations adjacent to helix D. PMID: 24068708
  45. Prevalence of inherited antithrombin mutations in thrombosis patients is higher than previously estimated. PMID: 23429250
  46. analysis of compound heterozygosty of SERPINC1 in antithrombin deficiency [case reports] PMID: 23329010
  47. A novel function for AT, which accelerates the modulation of FXa into the fibrinolytic form. PMID: 23416531
  48. Data suggest that plasma FVIIa-AT complex (coagulation factor VII-antithrombin III) is higher in portal vein thrombosis (PVT; without cirrhosis) than in healthy subjects; no difference in FVIIa-AT complex is observed in cirrhosis with/without PVT. PMID: 22958499
  49. A novel heterozygous mutation on exon 5 (c.1009C > T p.Q337X)of the SerpinC1 gene was identified in two half-siblings with neonatal cerebral sinus venous thrombosis. PMID: 22997155
  50. The serum ATIII level before hepatectomy in hepatocellular carcinoma is valuable to estimate the pathological background and predict postoperative liver failure/ dysfunction. PMID: 22353523

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Involvement in disease
Antithrombin III deficiency (AT3D)
Subcellular Location
Secreted, extracellular space.
Protein Families
Serpin family
Tissue Specificity
Found in plasma.
Database Links

HGNC: 775

OMIM: 107300

KEGG: hsa:462

STRING: 9606.ENSP00000356671

UniGene: Hs.75599

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